eF-site ID 4u1r-A PDB Code 4u1r Chain A click to enlarge Title ATP-bound structure of human platelet phosphofructokinase in an R-state, crystal form II Classification TRANSFERASE Compound ATP-dependent 6-phosphofructokinase, platelet type Source Homo sapiens (Human) (PFKAP_HUMAN) Sequence A:  SAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFIYEGY QGMVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTR EGRLKAACNLLQRGITNLCVIGGDGSLTGANLFRKEWSGL LEELARNGQIDKEAVQKYAYLNVVGMVGSIDNDFCGTDMT IGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYL ALVSALACGADWVFLPESPPEEGWEEQMCVKLSENRARKK RLNIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDTRVTI LGHVQRGGTPSAFDRILASRMGVEAVIALLEATPDTPACV VSLNGNHAVRLPLMECVQMTQDVQKAMDERRFQDAVRLRG RSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVINVGAPAAG MNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWT DVGGWTGQGGSILGTKRVLPGKYLEEIATQMRTHSINALL IIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVSNNVP GSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMG GYCGYLANMGGLAAGADAAYIFEEPFDIRDLQSNVEHLTE KMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKGVFDC RKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKEA RFTTDDSICVLGISKRNVIFQPVAELKKQTDFEHRIPKEQ WWLKLRPLMKILA Description (1)  human platelet phosphofructokinase Functional site 1) chain A residue 32 type sequence S description binding site for residue ATP A 801 source : AC1 2) chain A residue 33 type sequence G description binding site for residue ATP A 801 source : AC1 3) chain A residue 34 type sequence G description binding site for residue ATP A 801 source : AC1 4) chain A residue 64 type sequence Y description binding site for residue ATP A 801 source : AC1 5) chain A residue 97 type sequence R description binding site for residue ATP A 801 source : AC1 6) chain A residue 98 type sequence C description binding site for residue ATP A 801 source : AC1 7) chain A residue 101 type sequence F description binding site for residue ATP A 801 source : AC1 8) chain A residue 102 type sequence R description binding site for residue ATP A 801 source : AC1 9) chain A residue 127 type sequence G description binding site for residue ATP A 801 source : AC1 10) chain A residue 128 type sequence D description binding site for residue ATP A 801 source : AC1 11) chain A residue 129 type sequence G description binding site for residue ATP A 801 source : AC1 12) chain A residue 130 type sequence S description binding site for residue ATP A 801 source : AC1 13) chain A residue 133 type sequence G description binding site for residue ATP A 801 source : AC1 14) chain A residue 233 type sequence G description binding site for residue PO4 A 802 source : AC2 15) chain A residue 264 type sequence K description binding site for residue PO4 A 802 source : AC2 16) chain A residue 430 type sequence R description binding site for residue PO4 A 802 source : AC2 17) chain A residue 434 type sequence R description binding site for residue PO4 A 802 source : AC2 18) chain A residue 467 type sequence G description binding site for residue PO4 A 802 source : AC2 19) chain A residue 468 type sequence G description binding site for residue PO4 A 802 source : AC2 20) chain A residue 576 type sequence R description binding site for residue PO4 A 803 source : AC3 21) chain A residue 665 type sequence R description binding site for residue PO4 A 803 source : AC3 22) chain A residue 44 type sequence R description binding site for residue PO4 A 804 source : AC4 23) chain A residue 48 type sequence R description binding site for residue PO4 A 804 source : AC4 24) chain A residue 83 type sequence S description binding site for residue PO4 A 804 source : AC4 25) chain A residue 84 type sequence S description binding site for residue PO4 A 804 source : AC4 26) chain A residue 599 type sequence G description binding site for residue PO4 A 804 source : AC4 27) chain A residue 632 type sequence R description binding site for residue PO4 A 804 source : AC4 28) chain A residue 481 type sequence R description binding site for residue PO4 A 805 source : AC5 29) chain A residue 671 type sequence H description binding site for residue PO4 A 805 source : AC5 30) chain A residue 301-319 type prosite sequence RVTILGHVQRGGTPSAFDR description PHOSPHOFRUCTOKINASE Phosphofructokinase signature. RvtilGHvQRGGtpsafDR source prosite : PS00433 31) chain A residue 665-683 type prosite sequence RKNVLGHMQQGGAPSPFDR description PHOSPHOFRUCTOKINASE Phosphofructokinase signature. RvtilGHvQRGGtpsafDR source prosite : PS00433 32) chain A residue 175 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 127 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 128 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 210 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 36) chain A residue 301 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 576 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 38) chain A residue 665 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 34 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 40) chain A residue 97 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 41) chain A residue 273 type BINDING sequence E description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 42) chain A residue 307 type BINDING sequence H description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 43) chain A residue 744 type BINDING sequence R description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 44) chain A residue 481 type BINDING sequence R description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 45) chain A residue 538 type BINDING sequence T description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 46) chain A residue 583 type BINDING sequence M description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 47) chain A residue 639 type BINDING sequence E description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 48) chain A residue 671 type BINDING sequence H description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 49) chain A residue 173 type BINDING sequence S description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 50) chain A residue 217 type BINDING sequence M description in other chain => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI3 51) chain A residue 142 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P47860 source Swiss-Prot : SWS_FT_FI4 52) chain A residue 688 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 53) chain A residue 395 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 54) chain A residue 486 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 55) chain A residue 386 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:33607258, ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 56) chain A residue 651 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI7 57) chain A residue 540 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI8

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